Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum.

@article{Kohlstock2001Cys359OG,
  title={Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum.},
  author={U M Kohlstock and Karl Peter Ruecknagel and Michael Reuter and Angelika Schierhorn and Jan Remmer Andreesen and Brigitte S{\"o}hling},
  journal={European journal of biochemistry},
  year={2001},
  volume={268 24},
  pages={6417-25}
}
In the amino-acid-fermenting anaerobe Eubacterium acidaminophilum, acetyl phosphate is synthesized by protein C of glycine reductase from a selenoprotein A-bound carboxymethyl-selenoether. We investigated specific thiols present in protein C for responsibility for acetyl phosphate liberation. After cloning of the genes encoding the large and the small subunit (grdC1, grdD1), they were expressed separately in Escherichia coli and purified as Strep-tag proteins. GrdD was the only subunit that… CONTINUE READING